The binding of human liver acid beta-galactosidase to wheat-germ lectin is influenced by aggregation state of the enzyme.
At low ionic strength and pH 6.0 human liver acid beta-galactosidase exists in two aggregation states, monomeric and multimeric. These species can be separated on wheat-germ lectin-Sepharose, Cellogel electrophoresis and gel filtration on Sephadex G-200, and are not normally interconvertible. On re-application of either form to wheat-germ lectin-Sepharose the equilibrium is re-established and the two forms are interconverted.
D001665:Binding Sites; D002847:Chromatography, Agarose; D002850:Chromatography, Gel; D004586:Electrophoresis; D005696:Galactosidases / Q000378:metabolism*; D006801:Humans; D037102:Lectins / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D011485:Protein Binding; D014909:Wheat Germ Agglutinins; D001616:beta-Galactosidase / Q000378:metabolism*
D037102:Lectins; D046911:Macromolecular Substances; D014909:Wheat Germ Agglutinins; D005696:Galactosidases; D001616:beta-Galactosidase